ID A8PWZ5_MALGO Unreviewed; 395 AA.
AC A8PWZ5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=MGL_1271 {ECO:0000313|EMBL:EDP44789.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44789.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44789.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDP44789.1}.
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DR EMBL; AAYY01000003; EDP44789.1; -; Genomic_DNA.
DR RefSeq; XP_001732003.1; XM_001731951.1.
DR AlphaFoldDB; A8PWZ5; -.
DR STRING; 425265.A8PWZ5; -.
DR GeneID; 5856308; -.
DR KEGG; mgl:MGL_1271; -.
DR VEuPathDB; FungiDB:MGL_1271; -.
DR InParanoid; A8PWZ5; -.
DR OMA; WPEAEHF; -.
DR OrthoDB; 2715841at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..395
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 395 AA; 44194 MW; 7E310651DA880F9B CRC64;
MLLPVGHGLC SSVYKAPMHG ARIMEREGGV PNFVCIKQVD VDVQSAPHNV QREVALLQRT
RHMNLALLLA VFTDSPDHFT TIYNVVMPLY PIHLPDILNS TCARPSSLSM AELAEQDEPW
LHVLGFQTYS SFVLSSLRQL VEAVAHLHHE QIAHRDLKPS NIMFGIDGTL KLIDLGVAWE
VGMHETPPFG RRPSEGSTDC AIISDVGSGA FRAPELLFAP KNGYNAFQAD MWSLGTVLAG
FFTSLDEEPV QSLGADFLPW ERELFPDRPT HPELSRLRPR AYHRATLFDS SSGDITLACD
IFKGSGDSQR DESDWPEAAH FQPPLHDFPF MHGPAKESLL DRLPTWAQLS EVDTSQASQF
LKTFLPYWLP RLLELSAARR PSIDDLLEHL RHPIP
//
